(1) Department of Chemistry, St. John's University, 11439 Jamaica, New York, (USA);(2) Department of Industrial Pharmacy, College of Pharmacy and Allied Health, St. John's University, 11439 Jamaica, New York, (USA)
Abstract:
Summary Molecular interaction between uni-uni valent ions and bovine serum albumin was investigated by size-exclusion chromatography. Elution profiles are first presented for salt and protein solutions as samples with water as the mobile phase; then for water and protein as samples with salt solutions as the mobile phase. The results suggest the existence of a dynamic equilibrium between the salt ions and the protein ions as reactants and the ion-pair (salt-protein) complex as a product.